PLCG2
From Wikipedia, the free encyclopedia
Phospholipase C, gamma 2 (phosphatidylinositol-specific)
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Identifiers | |||||||||||
Symbol(s) | PLCG2; | ||||||||||
External IDs | OMIM: 600220 MGI: 97616 HomoloGene: 55671 | ||||||||||
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RNA expression pattern | |||||||||||
Orthologs | |||||||||||
Human | Mouse | ||||||||||
Entrez | 5336 | 234779 | |||||||||
Ensembl | ENSG00000197943 | ENSMUSG00000034330 | |||||||||
Uniprot | P16885 | n/a | |||||||||
Refseq | NM_002661 (mRNA) NP_002652 (protein) |
NM_172285 (mRNA) NP_758489 (protein) |
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Location | Chr 16: 80.37 - 80.55 Mb | Chr 8: 120.38 - 120.52 Mb | |||||||||
Pubmed search | [1] | [2] |
Phospholipase C, gamma 2 (phosphatidylinositol-specific), also known as PLCG2, is a human gene.[1]
Enzymes of the phospholipase C family catalyze the hydrolysis of phospholipids to yield diacylglycerols and water-soluble phosphorylated derivatives of the lipid head groups. A number of these enzymes have specificity for phosphoinositides. Of the phosphoinositide-specific phospholipase C enzymes, C-beta is regulated by heterotrimeric G protein-coupled receptors, while the closely related C-gamma-1 (PLCG1; MIM 172420) and C-gamma-2 enzymes are controlled by receptor tyrosine kinases. The C-gamma-1 and C-gamma-2 enzymes are composed of phospholipase domains that flank regions of homology to noncatalytic domains of the SRC oncogene product, SH2 and SH3.[supplied by OMIM][1]
[edit] References
[edit] Further reading
- Fruman DA, Satterthwaite AB, Witte ON (2000). "Xid-like phenotypes: a B cell signalosome takes shape.". Immunity 13 (1): 1-3. PMID 10933389.
- Cefai D, Debre P, Kaczorek M, et al. (1991). "Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway.". J. Clin. Invest. 86 (6): 2117-24. PMID 1979339.
- Ohta S, Matsui A, Nazawa Y, Kagawa Y (1989). "Complete cDNA encoding a putative phospholipase C from transformed human lymphocytes.". FEBS Lett. 242 (1): 31-5. PMID 2849563.
- Yan W, Ratnam M (1995). "Preferred sites of glycosylphosphatidylinositol modification in folate receptors and constraints in the primary structure of the hydrophobic portion of the signal.". Biochemistry 34 (44): 14594-600. PMID 7578066.
- Zauli G, Previati M, Caramelli E, et al. (1995). "Exogenous human immunodeficiency virus type-1 Tat protein selectively stimulates a phosphatidylinositol-specific phospholipase C nuclear pathway in the Jurkat T cell line.". Eur. J. Immunol. 25 (9): 2695-700. PMID 7589147.
- Liao F, Shin HS, Rhee SG (1993). "In vitro tyrosine phosphorylation of PLC-gamma 1 and PLC-gamma 2 by src-family protein tyrosine kinases.". Biochem. Biophys. Res. Commun. 191 (3): 1028-33. doi: . PMID 7682059.
- Hernandez D, Egan SE, Yulug IG, Fisher EM (1995). "Mapping the gene that encodes phosphatidylinositol-specific phospholipase C-gamma 2 in the human and the mouse.". Genomics 23 (2): 504-7. doi: . PMID 7835906.
- Daniel JL, Dangelmaier C, Smith JB (1994). "Evidence for a role for tyrosine phosphorylation of phospholipase C gamma 2 in collagen-induced platelet cytosolic calcium mobilization.". Biochem. J. 302 ( Pt 2): 617-22. PMID 8093016.
- Obermeier A, Lammers R, Wiesmüller KH, et al. (1993). "Identification of Trk binding sites for SHC and phosphatidylinositol 3'-kinase and formation of a multimeric signaling complex.". J. Biol. Chem. 268 (31): 22963-6. PMID 8226808.
- Pleiman CM, Clark MR, Gauen LK, et al. (1993). "Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase.". Mol. Cell. Biol. 13 (9): 5877-87. PMID 8395016.
- Sidorenko SP, Law CL, Klaus SJ, et al. (1996). "Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling.". Immunity 5 (4): 353-63. PMID 8885868.
- Kang JS, Kohlhuber F, Hug H, et al. (1997). "Cloning and functional analysis of the hematopoietic cell-specific phospholipase C(gamma)2 promoter.". FEBS Lett. 399 (1-2): 14-20. PMID 8980110.
- Chen P, Mayne M, Power C, Nath A (1997). "The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases.". J. Biol. Chem. 272 (36): 22385-8. PMID 9278385.
- Cunningham SA, Arrate MP, Brock TA, Waxham MN (1998). "Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites.". Biochem. Biophys. Res. Commun. 240 (3): 635-9. doi: . PMID 9398617.
- Mayne M, Bratanich AC, Chen P, et al. (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease.". Neuroimmunomodulation 5 (3-4): 184-92. PMID 9730685.
- Bai RY, Dieter P, Peschel C, et al. (1998). "Nucleophosmin-anaplastic lymphoma kinase of large-cell anaplastic lymphoma is a constitutively active tyrosine kinase that utilizes phospholipase C-gamma to mediate its mitogenicity.". Mol. Cell. Biol. 18 (12): 6951-61. PMID 9819383.
- Tomassetti A, Bottero F, Mazzi M, et al. (1999). "Molecular requirements for attachment of the glycosylphosphatidylinositol anchor to the human alpha folate receptor.". J. Cell. Biochem. 72 (1): 111-8. PMID 10025672.
- Shen Z, Batzer A, Koehler JA, et al. (1999). "Evidence for SH3 domain directed binding and phosphorylation of Sam68 by Src.". Oncogene 18 (33): 4647-53. doi: . PMID 10467411.
- Gross BS, Melford SK, Watson SP (1999). "Evidence that phospholipase C-gamma2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets.". Eur. J. Biochem. 263 (3): 612-23. PMID 10469124.
- Haughey NJ, Holden CP, Nath A, Geiger JD (1999). "Involvement of inositol 1,4,5-trisphosphate-regulated stores of intracellular calcium in calcium dysregulation and neuron cell death caused by HIV-1 protein tat.". J. Neurochem. 73 (4): 1363-74. PMID 10501179.